6MWB: Ion transport protein

NavAb Voltage-gated Sodium Channel, residues 1-239 with mutation T206A. Determined by X-ray diffraction at 2.6 Å resolution. Released 19 Dec 2018.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Arcobacter butzleri (strain RM4018)
Chains
1
Atoms
2,126
Mol. weight
33.8 kDa
Ligands
CPS, PX4
Released
19 Dec 2018

Explore 6MWB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6MWB contains 15 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain B: 15 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix2000-201011
α-helix2012-203120
α-helix2035-206733
α-helix2068-20714
α-helix2075-208612
α-helix2097-21015
α-helix2102-21076
α-helix2108-21114
α-helix2114-212512
α-helix2127-215226
α-helix2157-21604
α-helix2163-217412
α-helix2179-21846
α-helix2185-21906
α-helix2195-223844

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ion transport proteinBprotein257Arcobacter butzleri (strain RM4018)A8EVM5 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>6MWB_1 Ion transport protein (chains B)
MDYKDDDDKGSLVPRGSHMYLRITNIVESSFFTKFIIYLIVLNGITMGLETSKTFMQSFG
VYTTLFNQIVITIFTIEIILRIYVHRISFFKDPWSLFDFFVVAISLVPTSSGFEILRVLR
VLRLFRLVTAVPQMRKIVSALISVIPGMLSVIALMTLFFYIFAIMATQLFGERFPEWFGT
LGESFYTLFQVMTLESWSMGIVRPLMEVYPYAWVFFIPFIFVVAFVMINLVVAIIVDAMA
ILNQKEEQHIIDEVQSH

Ligands and cofactors

IDNameFormulaCopies
CPS3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonateC32 H58 N2 O7 S2
PX41,2-dimyristoyl-sn-glycero-3-phosphocholineC36 H73 N O8 P4

Water and common crystallization additives (SO4) are not listed.

Primary citation

Molecular dissection of multiphase inactivation of the bacterial sodium channel NaVAb. Gamal El-Din, T.M., Lenaeus, M.J., Ramanadane, K. et al. J Gen Physiol (2019) 151:174-185. DOI 10.1085/jgp.201711884 · PubMed

Other PDB entries of the same protein (UniProt A8EVM5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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